BMRB Entry 15397

Name: NH, NN, C, CA and CB chemical shift assignment of the transcriptional activation domain 1 of the nuclear hormone receptor coactivator ACTR in the free state
Published: 2008-04-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15397

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NH, NN, C, CA and CB chemical shift assignment of the transcriptional activation domain 1 of the nuclear hormone receptor coactivator ACTR in the free state

Deposition date:

2007-07-20

Original release date:

2008-04-04

Authors:

Ebert, Marc-Olivier; Bae, Sung-Hun; Dyson, H.; Wright, Peter

Citation:

Citation: Ebert, Marc-Olivier; Bae, Sung-Hun; Dyson, H.; Wright, Peter. "NMR Relaxation Study of the Complex Formed Between CBP and the Activation Domain of the Nuclear Hormone Receptor Coactivator ACTR" Biochemistry 47, 1299-1308 (2008).
PubMed: 18177052

Assembly members:

Assembly members:
ACTR, polymer, 71 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ACTR: GTQNRPLLRNSLDDLVGPPS NLEGQSDERALLDQLHTLLS NTDATGLEEIDRALGIPELV NQGQALEPKQD

Data sets:

assigned_chemical_shifts
- NH_NN_C_CA_and_CB_shifts

Data type	Count
13C chemical shifts	182
15N chemical shifts	62
1H chemical shifts	62

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ACTR	1

Entities:

Entity 1, ACTR 71 residues - Formula weight is not available

1

GLY

THR

GLN

ASN

ARG

PRO

LEU

ARG

ASN

2

SER

LEU

ASP

LEU

VAL

GLY

PRO

SER

3

ASN

LEU

GLU

GLY

GLN

SER

ASP

GLU

ARG

ALA

4

LEU

ASP

GLN

LEU

HIS

THR

LEU

SER

5

ASN

THR

ASP

ALA

THR

GLY

LEU

GLU

ILE

6

ASP

ARG

ALA

LEU

GLY

ILE

PRO

GLU

LEU

VAL

7

ASN

GLN

GLY

GLN

ALA

LEU

GLU

PRO

LYS

GLN

8

ASP

Samples:

sample_1: ACTR, [U-98% 13C; U-98% 15N], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.7; pressure: 1 atm; temperature: 304.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (HCA)CO(CA)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker DRX 750 MHz
Bruker DRX 600 MHz
Bruker DRX 500 MHz

PDB	1KBH
DBJ	BAD93100 BAF82372 BAG10971 BAG63847
GB	AAB92368 AAC51663 AAC51677 AAC51849 AAH92516
REF	NP_001107748 NP_001167558 NP_001167559 NP_006525 NP_858045
SP	Q9Y6Q9
TPG	DAA23082
AlphaFold	Q9Y6Q9